ArticleJournal of proteome research2011
Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Tyrosine Kinase Receptors, Inhibition, and Potential Role in the Pharmacotherapy of Retinal Disorders.Ophthalmology and therapy · 2026Review
- LKB1-MARK2 signalling mediates lipopolysaccharide-induced production of cytokines in mouse macrophages.Journal of cellular and molecular medicine · 2020Article
- Don't forget astrocytes when targeting Alzheimer's disease.British journal of pharmacology · 2019Review
- The vimentin intermediate filament network restrains regulatory T cell suppression of graft-versus-host disease.The Journal of clinical investigation · 2018Article
- Sample Preparation for Relative Quantitation of Proteins Using Tandem Mass Tags (TMT) and Mass Spectrometry (MS).Methods in molecular biology (Clifton, N.J.) · 2018Article
- Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea.Journal of cellular and molecular medicine · 2017Article
- Deep Coverage of Global Protein Expression and Phosphorylation in Breast Tumor Cell Lines Using TMT 10-plex Isobaric Labeling.Journal of proteome research · 2017Article
- Oncogenic KIT mutations in different exons lead to specific changes in melanocyte phospho-proteome.Journal of proteomics · 2016Article
- Comparing multistep immobilized metal affinity chromatography and multistep TiO2 methods for phosphopeptide enrichment.Analytical chemistry · 2015Article
- Global analysis of muscle-specific kinase signaling by quantitative phosphoproteomics.Molecular & cellular proteomics : MCP · 2014Article
- Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Quantitative analysis of global phosphorylation changes with high-resolution tandem mass spectrometry and stable isotopic labeling.Methods (San Diego, Calif.) · 2013Review
- Analysis of SRC oncogenic signaling in colorectal cancer by stable isotope labeling with heavy amino acids in mouse xenografts.Molecular & cellular proteomics : MCP · 2012Article
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2 authors.
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Abstract
There are three quantitative phosphoproteomic strategies most commonly used to study receptor tyrosine kinase (RTK) signaling. These strategies quantify changes in: (1) all three forms of phosphosites (phosphoserine, phosphothreonine and phosphotyrosine) following enrichment of phosphopeptides by titanium dioxide or immobilized metal affinity chromatography; (2) phosphotyrosine sites following anti- phosphotyrosine antibody enrichment of phosphotyrosine peptides; or (3) phosphotyrosine proteins and their binding partners following anti-phosphotyrosine protein immunoprecipitation. However, it is not clear from literature which strategy is more effective. In this study, we assessed the utility of these three phosphoproteomic strategies in RTK signaling studies by using EphB receptor signaling as an example. We used all three strategies with stable isotope labeling with amino acids in cell culture (SILAC) to compare changes in phosphoproteomes upon EphB receptor activation. We used bioinformatic analysis to compare results from the three analyses. Our results show that the three strategies provide complementary information about RTK pathways.
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